Purification and characterization of a collagenolytic serine proteinase from the skeletal muscle of red sea bream (Pagrus major)

Wu, Guoping; Chen, Suhua; Yoshida, Asami; Zhang, Ling‐Jing; Su, Wen‐Jin; Cao, Min‐Jie

doi:10.1016/j.cbpb.2009.11.014

Cited by 25 publications

(36 citation statements)

References 32 publications

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“…In relation to the susceptibility to metal ions, the data obtained from our study corroborate those reported by KIM et al (2002) andWU et al (2010a) which observed increased activity of collagenolytic proteases of filefish N. modestrus and sea bream P. major when exposed to the ions Ca 2+ and Mg 2+ , respectively. HAYET et al (2011) .…”

Section: Sensitivity Of the Collagenolytic Enzymes To Metal Ions And supporting

confidence: 90%

“…The optimum pH values presented in this study are in conformity to those reported for other fish species, such as: N. modestrus filefish , sea bream P. major (WU et al, 2010a) and sardinelle S. aurita (HAYET et al, 2011). TERUEL andSIMPSON (1995), BYUN et al (2002), , SOUCHET andLAPLANTE (2011) andDABOOR et al (2012) reported an optimum pH of 7.5 to enzymes obtained from the aquatic species: winter flounder (P. americanus), tuna (T. thymus), Mackerel (S. japonicus), snow crab (Chionoecetes opilio) and fish waste, respectively.…”

Section: Temperature and Ph Assay Of The Collagenolytic Enzymesupporting

confidence: 90%

“…The optimum temperature depends on the type of enzyme, the analyzed tissue and the source species, and has been reported for collagenolytic enzymes in the range of 30°C and 60°C PARK et al, 2002;DABOOR et al, 2012;WU et al, 2010a;HAYET et al, 2011;SUPHATHARAPRATEEP et al, 2011;BAEHAKI et al, 2012;LIMA et al, 2013). Similar results to the present study were described for winter flounder P. americanus (TERUEL and SIMPSON 1995), filefish species N. modestrus , tuna T.…”

Section: Temperature and Ph Assay Of The Collagenolytic Enzymesupporting

confidence: 90%

“…HAYET et al (2011) . ROY et al (1996), BYUN et al (2002, KIM et al (2002) andWU et al (2010a) also observed increased activity of collagenolytic proteases from greenshore crab (C. maenas), tuna (T. thymus), mackerel (S. japonicus), filefish (N. modestrus) and sea bream P. major in the presence of the ions Ca 2+ and Mg…”

Section: Sensitivity Of the Collagenolytic Enzymes To Metal Ions And mentioning

confidence: 73%

“…MUKHERJEE et al (2009) observed that pH 5.0 improved the activity of enzymes from species of sponge (R. odorabile). The stability of pH has also been reported for aquatic species such as fish, crustaceans, and sponges, and optimal values were found oscillating between < 5.0 and > 10.0 (TURKIEWIC et al, 1991;KRISTJÁMSSON et al, 1995;TERUEL and SIMPSON, 1995;MURADO et al, 2009;WU et al, 2010a;WU et al, 2010b;HAYET et al, 2011;SOUCHET and LAPLANTE, 2011;SUPHATHARAPRATEEP et al, 2011;BAEHAKI et al, 2012).…”

Section: Temperature and Ph Assay Of The Collagenolytic Enzymementioning

confidence: 91%

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Colagenase de pescada branca: extração, purificação parcial, caracterização e teste de especificidade ao colágeno para aplicação industrial

et al. 2017

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Fish processing residues are rich sources of biomolecules with industrial potential, such as enzymes with collagenolytic properties applied in the pharmaceutical, textile and leather sectors. Here, collagenolytic serine proteases were partially purified from the waste (viscera) of smooth weakfish Cynoscion leiarchus and characterized for the purpose of obtaining a value-added product from fisheries resources. The higher activity of the enzyme (72.5 U mL -1 ) was verified in optimal temperature and pH of 55°C and 8.0, respectively. The enzyme was stable in wide ranges of temperature (25-60°C) and pH (6.5 to 11.5). The ions Ca 2+ and Mg 2+ increased the protease activity, whilst Pb 2+, Al 3+ and Cu 2+ had an inhibitory effect, as observed in the presence of Benzamidine and TLCK (inhibitors of serine proteases). Hydrolysis was detected after 48 hours, when the enzyme and bovine collagen type I were incubated together. Thus, digestive viscera of C. leiarchus is suggested as an alternative source of enzymes capable of cleaving type I collagen, with similar biochemical properties to bacterial collagenases commonly employed in industrial processes, reducing costs, adding value to the fisheries product and minimizing the environmental impact caused by its waste. , com temperatura e pH ótimos de 55°C e 8.0, respectivamente. A enzima manteve-se estável em faixas amplas de temperatura (25-60 °C) e pH (6,(5)(6)(7)(8)(9)(10)(11)5 , Al 3+ e Cu 2+ inibiram essa atividade assim como os inibidores de serino-proteases (Benzamidina e TLCK). A hidrólise foi detectada após 48h de incubação com colágeno bovino tipo I. Assim, sugere-se vísceras digestivas de C. leiarchus como fonte alternativa para o fornecimento de enzimas com capacidade de clivar o colágeno do tipo I e com propriedades bioquímicas semelhantes às colagenases bacterianas já empregadas nas etapas de processamento industrial, como forma de redução de custo, agregação de valor ao produto pesqueiro e contribuindo para minimizar o impacto ambiental deste tipo de resíduo.

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Section: Sensitivity Of the Collagenolytic Enzymes To Metal Ions And supporting

confidence: 90%